SRP1_SCHPO
ID SRP1_SCHPO Reviewed; 275 AA.
AC Q10193; O74305;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 15-JUL-1999, sequence version 3.
DT 03-AUG-2022, entry version 144.
DE RecName: Full=Pre-mRNA-splicing factor srp1;
GN Name=srp1; ORFNames=SPBC11C11.08;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PHOSPHORYLATION.
RC STRAIN=972 / ATCC 24843;
RX PubMed=9421507; DOI=10.1093/nar/26.2.505;
RA Gross T., Richert K., Mierke C., Luetzelberger M., Kaeufer N.F.;
RT "Identification and characterization of srp1, a gene of fission yeast
RT encoding a RNA binding domain and a RS domain typical of SR splicing
RT factors.";
RL Nucleic Acids Res. 26:505-511(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-115; SER-117; SER-119;
RP SER-125; SER-127; TYR-129; SER-154; SER-156; TYR-159; SER-170; SER-172 AND
RP SER-181, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
CC -!- FUNCTION: Has a role in pre-mRNA splicing where it is involved in
CC spliceosome assembly. {ECO:0000269|PubMed:9421507}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC -!- PTM: Extensively phosphorylated by prp4 on serine residues in the RS
CC domain. {ECO:0000269|PubMed:18257517, ECO:0000269|PubMed:9421507}.
CC -!- SIMILARITY: Belongs to the splicing factor SR family. {ECO:0000305}.
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DR EMBL; U66833; AAC49909.1; -; Genomic_DNA.
DR EMBL; CU329671; CAA20690.1; -; Genomic_DNA.
DR PIR; T48696; T48696.
DR RefSeq; NP_596398.1; NM_001022318.2.
DR AlphaFoldDB; Q10193; -.
DR SMR; Q10193; -.
DR BioGRID; 276368; 89.
DR STRING; 4896.SPBC11C11.08.1; -.
DR iPTMnet; Q10193; -.
DR PaxDb; Q10193; -.
DR PRIDE; Q10193; -.
DR EnsemblFungi; SPBC11C11.08.1; SPBC11C11.08.1:pep; SPBC11C11.08.
DR GeneID; 2539818; -.
DR KEGG; spo:SPBC11C11.08; -.
DR PomBase; SPBC11C11.08; srp1.
DR VEuPathDB; FungiDB:SPBC11C11.08; -.
DR eggNOG; ENOG502S4TA; Eukaryota.
DR HOGENOM; CLU_082818_0_0_1; -.
DR InParanoid; Q10193; -.
DR OMA; HERDYER; -.
DR PRO; PR:Q10193; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0005737; C:cytoplasm; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; IDA:PomBase.
DR GO; GO:0003723; F:RNA binding; ISM:PomBase.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; TAS:PomBase.
DR CDD; cd12467; RRM_Srp1p_like; 1.
DR Gene3D; 3.30.70.330; -; 1.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034403; Srp1p_RRM.
DR Pfam; PF00076; RRM_1; 1.
DR SMART; SM00360; RRM; 1.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 1.
PE 1: Evidence at protein level;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; RNA-binding.
FT CHAIN 1..275
FT /note="Pre-mRNA-splicing factor srp1"
FT /id="PRO_0000081962"
FT DOMAIN 7..86
FT /note="RRM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 79..275
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 95..167
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 169..189
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 190..204
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..232
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 243..275
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 115
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 117
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 119
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 125
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 127
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 129
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 154
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 156
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 159
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 170
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 181
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT CONFLICT 230
FT /note="G -> C (in Ref. 1; AAC49909)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 275 AA; 31069 MW; 0FA4EAF6EBB249CE CRC64;
MSRRSLRTLY VTGFRDGMRA RELAYEFEPF GPLIRCDIPI PRTRTSRPFA FVEYEDSRDA
EDAYYEVHGR RLERGGGVLR VEWAKQPPPS GPGSKRGGRR ERGGRVHGDS GRLRSRSPSP
HEARSRSPYN DERSDRRSMS PRYRSRSRSP DGRSRSPDYD RRSPKRNHRS PSPVSFAPQK
SPVENETETN VDNGDTKISE SNEKSGTEVE QQSAPNSNGN EEVNNLEPVG QNESKQEPPK
EENSNVSQEQ PEQAQPEVSA ASEQPESNPT TTESQ
